Analytical Data
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Gene name
ALG8
- Application
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Alternative Names
ALG8; HUSSY-02Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1.3-glucosyltransferase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BVK2
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Expression Region
1-526aa
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AA Sequence
MAALTIATGTGNWFSALALGVTLLKCLLIPTYHSTDFEVHRNWLAITHSLPISQWYYEATSEWTLDYPPFFAWFEYILSHVAKYFDQEMLNVHNLNYSSSRTLLFQRFSVIFMDVLFVYAVRECCKCIDGKKVGKELTEKPKFILSVLLLWNFGLLIVDHIHFQYNGFLFGLMLLSIARLFQKRHMEGAFLFAVLLHFKHIYLYVAPAYGVYLLRSYCFTANKPDGSIRWKSFSFVRVISLGLVVFLVSALSLGPFLALNQLPQVFSRLFPFKRGLCHAYWAPNFWALYNALDKVLSVIGLKLKFLDPNNIPKASMTSGLVQQFQHTVLPSVTPLATLICTLIAILPSIFCLWFKPQGPRGFLRCLTLCALSSFMFGWHVHEKAILLAILPMSLLSVGKAGDASIFLILTTTGHYSLFPLLFTAPELPIKILLMLLFTIYSISSLKTLFRKEKPLFNWMETFYLLGLGPLEVCCEFVFPFTSWKVKYPFIPLLLTSVYCAVGITYAWFKLYVSVLIDSAIGKTKKQ
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Molecular Weight
60 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
ALG8 is a key player in the biosynthesis of N-glycans, specifically in the assembly of the precursor oligosaccharide that is transferred to nascent polypeptides during protein synthesis. It encodes a glycosyltransferase that is crucial for the addition of mannose residues, which helps in the proper folding and quality control of glycoproteins within the endoplasmic reticulum. Mutations or dysfunctions in the ALG8 gene can lead to congenital disorders of glycosylation (CDG), resulting in serious developmental and cognitive impairments. Recent studies highlight the importance of ALG8 in various cellular processes beyond glycosylation, including implications in cellular stress responses and immune system modulation. The recombinant expression of ALG8 protein enables researchers to study its structural and functional properties, assess its role in glycoprotein maturation, and explore potential therapeutic avenues for CDG. Through high-throughput screening techniques and biochemical assays, investigators aim to uncover how variations in ALG8 function can affect glycan profiles and overall protein functionality, contributing to a deeper understanding of glycosylation disorders and paving the way for targeted drug development and personalized medicine strategies.
